ID A0A2K2HC03_9DELT Unreviewed; 804 AA. AC A0A2K2HC03; DT 28-MAR-2018, integrated into UniProtKB/TrEMBL. DT 28-MAR-2018, sequence version 1. DT 25-MAY-2022, entry version 18. DE RecName: Full=Lon protease {ECO:0000256|HAMAP-Rule:MF_01973, ECO:0000256|PIRNR:PIRNR001174}; DE EC=3.4.21.53 {ECO:0000256|HAMAP-Rule:MF_01973, ECO:0000256|PIRNR:PIRNR001174}; DE AltName: Full=ATP-dependent protease La {ECO:0000256|HAMAP-Rule:MF_01973}; GN Name=lon {ECO:0000256|HAMAP-Rule:MF_01973}; GN ORFNames=C2E25_05260 {ECO:0000313|EMBL:PNU20797.1}; OS Geothermobacter hydrogeniphilus. OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales; OC Geobacteraceae; Geothermobacter. OX NCBI_TaxID=1969733 {ECO:0000313|EMBL:PNU20797.1, ECO:0000313|Proteomes:UP000236340}; RN [1] {ECO:0000313|EMBL:PNU20797.1, ECO:0000313|Proteomes:UP000236340} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HR-1 {ECO:0000313|EMBL:PNU20797.1, RC ECO:0000313|Proteomes:UP000236340}; RA Smith H., Abuyen K., Tremblay J., Savalia P., Perez-Rodriguez I., RA Emerson D., Tully B., Amend J.; RT "Genome Sequence of Geothermobacter sp. HR-1 Iron Reducer from the Loihi RT Seamount."; RL Genome Announc. 0:0-0(2018). CC -!- FUNCTION: ATP-dependent serine protease that mediates the selective CC degradation of mutant and abnormal proteins as well as certain short- CC lived regulatory proteins. Required for cellular homeostasis and for CC survival from DNA damage and developmental changes induced by stress. CC Degrades polypeptides processively to yield small peptide fragments CC that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, CC site-specific manner. {ECO:0000256|HAMAP-Rule:MF_01973}. CC -!- CATALYTIC ACTIVITY: CC Reaction=Hydrolysis of proteins in presence of ATP.; EC=3.4.21.53; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01973, CC ECO:0000256|PIRNR:PIRNR001174, ECO:0000256|PROSITE-ProRule:PRU01122}; CC -!- SUBUNIT: Homohexamer. Organized in a ring with a central cavity. CC {ECO:0000256|HAMAP-Rule:MF_01973, ECO:0000256|PIRNR:PIRNR001174}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496, CC ECO:0000256|HAMAP-Rule:MF_01973, ECO:0000256|PIRNR:PIRNR001174}. CC -!- INDUCTION: By heat shock. {ECO:0000256|HAMAP-Rule:MF_01973}. CC -!- SIMILARITY: Belongs to the peptidase S16 family. {ECO:0000256|HAMAP- CC Rule:MF_01973, ECO:0000256|PIRNR:PIRNR001174, ECO:0000256|PROSITE- CC ProRule:PRU01122, ECO:0000256|RuleBase:RU000591}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:PNU20797.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; PPFX01000008; PNU20797.1; -; Genomic_DNA. DR EnsemblBacteria; PNU20797; PNU20797; C2E25_05260. DR Proteomes; UP000236340; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:UniProtKB-UniRule. DR GO; GO:0004176; F:ATP-dependent peptidase activity; IEA:UniProtKB-UniRule. DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:UniProtKB-UniRule. DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule. DR GO; GO:0034605; P:cellular response to heat; IEA:UniProtKB-UniRule. DR GO; GO:0006515; P:protein quality control for misfolded or incompletely synthesized proteins; IEA:UniProtKB-UniRule. DR Gene3D; 2.30.130.40; -; 1. DR Gene3D; 3.30.230.10; -; 1. DR Gene3D; 3.40.50.300; -; 1. DR HAMAP; MF_01973; lon_bact; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR003959; ATPase_AAA_core. DR InterPro; IPR027543; Lon_bac. DR InterPro; IPR004815; Lon_bac/euk-typ. DR InterPro; IPR008269; Lon_proteolytic. DR InterPro; IPR027065; Lon_Prtase. DR InterPro; IPR003111; Lon_prtase_N. DR InterPro; IPR046336; Lon_prtase_N_sf. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR008268; Peptidase_S16_AS. DR InterPro; IPR015947; PUA-like_sf. DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold. DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr. DR PANTHER; PTHR10046; PTHR10046; 1. DR Pfam; PF00004; AAA; 1. DR Pfam; PF05362; Lon_C; 1. DR Pfam; PF02190; LON_substr_bdg; 1. DR PIRSF; PIRSF001174; Lon_proteas; 1. DR SMART; SM00382; AAA; 1. DR SMART; SM00464; LON; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54211; SSF54211; 1. DR SUPFAM; SSF88697; SSF88697; 1. DR TIGRFAMs; TIGR00763; lon; 1. DR PROSITE; PS51787; LON_N; 1. DR PROSITE; PS51786; LON_PROTEOLYTIC; 1. DR PROSITE; PS01046; LON_SER; 1. PE 2: Evidence at transcript level; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_01973, KW ECO:0000256|PIRNR:PIRNR001174}; Coiled coil {ECO:0000256|SAM:Coils}; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01973}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01973, ECO:0000256|PIRNR:PIRNR001174}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01973, KW ECO:0000256|PIRNR:PIRNR001174}; KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|HAMAP-Rule:MF_01973}; KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|HAMAP- KW Rule:MF_01973}; KW Stress response {ECO:0000256|ARBA:ARBA00023016, ECO:0000256|HAMAP- KW Rule:MF_01973}. FT DOMAIN 18..209 FT /note="Lon N-terminal" FT /evidence="ECO:0000259|PROSITE:PS51787" FT DOMAIN 601..782 FT /note="Lon proteolytic" FT /evidence="ECO:0000259|PROSITE:PS51786" FT NP_BIND 363..370 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01973, FT ECO:0000256|PIRSR:PIRSR001174-2" FT COILED 197..217 FT /evidence="ECO:0000256|SAM:Coils" FT COILED 237..278 FT /evidence="ECO:0000256|SAM:Coils" FT ACT_SITE 688 FT /evidence="ECO:0000256|HAMAP-Rule:MF_01973, FT ECO:0000256|PIRSR:PIRSR001174-1" FT ACT_SITE 731 FT /evidence="ECO:0000256|HAMAP-Rule:MF_01973, FT ECO:0000256|PIRSR:PIRSR001174-1" SQ SEQUENCE 804 AA; 89876 MW; C8220C179F358695 CRC64; MTEILEDYSG QEPSAELLPL LPLRDIVIFP HMVTPLFVGR PRSINALEGA MEKDKLVFLA TQKDPKNDEP QAEDIYEIGT VGQVIQMLKL PDGTVKVLVE GKMRGHIQAM MERDDCYFVS IEALEDRDSG SAEIEALIRS VNDAFENYIN LSKKVPAEMV SSVKGISEAG RLADTIIAHL NVRIAEKQEI LATMDSVERL ENLLGLLERE VEILQIEKKI RSRVKNQMER SQKEYYLNEQ MRAIQKELGE KDEFKQELRE LEENIQQKKM SKEGTEKALA ELRKLKMMSP MSAEATVVRN YLDWLIALPW KKGTKDQLDI VHAEEVLEAD HYGLKKVKER ILEYLAVQSL AKKIKGPILC LVGPPGVGKT SLGRSIARAM GRKFVRISLG GVRDEAEIRG HRRTYIGAMP GKIIQGLRKA GVKNPVFLLD EIDKMSTDFR GDPSSALLEV LDPEQNASFG DHFLDVEYDL SGVMFVTTAN TLHNIPRPLQ DRMEIIRIEG YTEEEKLHIA RRYLAGKQLE AHGLSPDQVR FSDAAIYEIV RHYTREAGVR SLEREFATIC RKIAREVVKS RRKDRRFVVG GGQVKKYLGV PRFNFGVKEQ QNRVGLVTGL AWTEVGGELL TIEVVVLPGQ GKLTVTGKLG EVMRESAQAA MSYVRSRWRE LGLDKDFYHK LDIHIHVPEG AIPKDGPSAG ITMATALASA LTGRPVDRDV AMTGEITLQG RVLPIGGLKE KLLAARRGGI GRVLIPQENE KDLEEVPSQV RKDLEVVPVA HMDGVISAAL QVGKEDAVLG QSAYSESAEE AVRH //